1DYK

Laminin alpha 2 chain LG4-5 domain pair

1DYK の概要

• エントリーDOI: 10.2210/pdb1dyk/pdb
• 関連するPDBエントリー: 1QU0
• 分子名称: LAMININ ALPHA 2 CHAIN, CALCIUM ION (3 entities in total)
• 機能のキーワード: metal binding protein, laminin
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42823.73

構造登録者

Tisi, D.,Talts, J.F.,Timple, R.,Hohenester, E. (登録日: 2000-02-01, 公開日: 2001-02-04, 最終更新日: 2024-10-09)

主引用文献

Tisi, D.,Talts, J.F.,Timpl, R.,Hohenester, E.
Structure of the C-Terminal Laminin G-Like Domain Pair of the Laminin Alpha 2 Chain Harbouring Binding Sites for Alpha-Dystroglycan and Heparin
Embo J., 19:1432-, 2000

PubMed Abstract: The laminins are large heterotrimeric glycoproteins with fundamental roles in basement membrane architecture and function. The C-terminus of the laminin alpha chain contains a tandem of five laminin G-like (LG) domains. We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3 fragment. LG4 and LG5 are arranged in a V-shaped fashion related by a 110 degrees rotation about an axis passing near the domain termini. An extended N-terminal segment is disulfide bonded to LG5 and stabilizes the domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 A apart at the tips of the domains opposite the polypeptide termini. An extensive basic surface region between the calcium sites is proposed to bind alpha-dystroglycan and heparin. The LG4-LG5 structure was used to construct a model of the laminin LG1-LG5 tandem and interpret missense mutations underlying protein S deficiency.

PubMed: 10747011
DOI: 10.1093/EMBOJ/19.7.1432

実験手法

X-RAY DIFFRACTION (2 Å)